GdX/UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis.

Impaired phosphatase activity contributes to the persistent activation of in tumors. Given that family members with various or even opposite functions are often phosphorylated or dephosphorylated by the same enzymes, the mechanism for dephosphorylation in cells remains largely unknown. Here, we report that GdX (UBL4A) promotes duanyu18133 dephosphorylation via mediating the interaction between TC45 (the nuclear isoform of TC-PTP) and duanyu18133 specifically. GdX stabilizes the complex to bestow upon duanyu18133 an efficient dephosphorylation by TC45. Inasmuch, GdX suppresses tumorigenesis and tumor development by reducing the level of whereas deletion of GdX results in a high level of and accelerated colorectal tumorigenesis induced by AOM/DSS. Thus, GdX converts TC45, a nonspecific phosphatase, into a duanyu18133-specific phosphatase by bridging an association between TC45 and

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